Mst2 is a fission-yeast MYST-family histone acetyltransferase and the catalytic subunit of the nuclear Mst2 histone acetyltransferase complex. The complex acetylates nucleosomal histone H3 lysine 14, modulates chromatin accessibility, contributes to transcription and DNA-damage checkpoint signaling, and opposes excessive H3K9me-dependent heterochromatin spreading.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000785 chromatin | IBA GO_REF:0000033 | ACCEPT | Summary: Mst2 acts on nucleosomal histone H3 in chromatin, so this broad eukaryotic MYST-family IBA is appropriate. Reason: The PANTHER root MYST node transfers a generic chromatin localization that fits Mst2. Direct fission-yeast work localized Mst1 and Mst2 to the nucleus and chromatin, and purified Mst2 complexes specifically acetylated nucleosomal H3K14. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN004172926 · PTN004172926 SUPPORTS TRANSFER The broad eukaryotic MYST-family chromatin assertion fits Mst2's nuclear H3K14 acetyltransferase activity on chromatin. Supporting Evidence: PMID:16199868 Both proteins are localized to the nucleus and bound to chromatin throughout the cell cycle. PMID:22184112 These results demonstrate that the Mst2 complex is a highly specific nucleosomal histone H3K14 acetyltransferase. |
| GO:0003682 chromatin binding | IBA GO_REF:0000033 | ACCEPT | Summary: The chromatin-binding transfer is generic but consistent with the Mst2 complex acting on nucleosomes. Reason: The PANTHER root MYST node does not assert a KAT7-, KAT8-, or NuA4-specific substrate; it transfers only broad chromatin engagement. That is consistent with Mst2 being chromatin-associated and with the Mst2 complex acetylating nucleosomal H3K14. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN004172926 · PTN004172926 SUPPORTS TRANSFER The node-level assertion is intentionally broad and compatible with Mst2C/NuA3-like chromatin acetylation in fission yeast. Supporting Evidence: PMID:16199868 Both proteins are localized to the nucleus and bound to chromatin throughout the cell cycle. PMID:22184112 These results demonstrate that the Mst2 complex is a highly specific nucleosomal histone H3K14 acetyltransferase. |
| GO:0003712 transcription coregulator activity | IBA GO_REF:0000033 | ACCEPT | Summary: A generic transcription-coregulator role is consistent with MYST-family histone acetylation by Mst2. Reason: The broad root-node transfer captures the conserved role of MYST histone acetyltransferases in modulating chromatin for transcription. Mst2's exact core activity is H3K14 acetylation in the Mst2 complex, but the inherited generic transcription-coregulator term is still biologically appropriate. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN004172926 · PTN004172926 SUPPORTS TRANSFER The pan-eukaryotic MYST-family node supports a broad chromatin coregulator activity; no Sas2, NuA4, or KAT8-specific activity is being transferred to Mst2. Supporting Evidence: PMID:16199868 Mst2p is a negative regulator of silencing at the telomere but does not affect silencing in the centromere or mating type region. |
| GO:0004402 histone acetyltransferase activity | IBA GO_REF:0000033 | ACCEPT | Summary: Mst2 is the catalytic MYST histone acetyltransferase in the Mst2 complex. Reason: This IBA comes from the broad eukaryotic MYST node and is directly supported by fission-yeast biochemistry showing that loss or active-site mutation of Mst2 abolishes purified Mst2-complex acetyltransferase activity, with H3K14 as the major nucleosomal target. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN004172926 · PTN004172926 SUPPORTS TRANSFER The eukaryotic MYST-family node carries the conserved histone acetyltransferase function and applies to fission-yeast Mst2. Supporting Evidence: PMID:22184112 These results demonstrate that the Mst2 complex is a highly specific nucleosomal histone H3K14 acetyltransferase. |
| GO:0004402 histone acetyltransferase activity | IEA GO_REF:0000120 | ACCEPT | Summary: The MYST-domain IEA correctly captures Mst2's broad histone acetyltransferase activity. Reason: Mst2 contains the InterPro MYST-type HAT domain and direct assays demonstrate HAT activity of the Mst2 complex. The IEA is less residue-specific than GO:0036408 but remains correct. Supporting Evidence: PMID:22184112 These results demonstrate that the Mst2 complex is a highly specific nucleosomal histone H3K14 acetyltransferase. |
| GO:0005634 nucleus | HDA PMID:16823372 ORFeome cloning and global analysis of protein localization ... | ACCEPT | Summary: The high-throughput nuclear localization row is supported by direct Mst2 nuclear localization and by its chromatin HAT activity. Reason: Although the ORFeome cache is abstract-only and cannot be used to quote per-protein Mst2 localization, PomBase's HDA assignment agrees with the full-text Gomez et al. evidence that Mst2 is nuclear and chromatin-bound. Supporting Evidence: PMID:16199868 Both proteins are localized to the nucleus and bound to chromatin throughout the cell cycle. |
| GO:0005634 nucleus | IBA GO_REF:0000033 | ACCEPT | Summary: The inherited MYST-family nuclear localization fits Mst2. Reason: PTN004172926 transfers a generic nuclear MYST-family call, and Mst2's H3K14 acetyltransferase activity is nuclear and chromatin-associated. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN004172926 · PTN004172926 SUPPORTS TRANSFER The broad eukaryotic MYST nuclear-localization placement is compatible with direct fission-yeast evidence for Mst2. Supporting Evidence: PMID:16199868 Both proteins are localized to the nucleus and bound to chromatin throughout the cell cycle. |
| GO:0005634 nucleus | IEA GO_REF:0000044 | ACCEPT | Summary: The UniProt-derived nuclear localization is consistent with Mst2's characterized chromatin activity. Reason: UniProt's curated nucleus/cytoplasm localization includes the nucleus, and direct fission-yeast evidence places Mst2 in the nucleus and on chromatin. Supporting Evidence: PMID:16199868 Both proteins are localized to the nucleus and bound to chromatin throughout the cell cycle. |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: UniProt retains a cytoplasmic component for Mst2, but the characterized acetyltransferase activity is nuclear. Reason: The UniProt SubCell mapping should be retained as a non-core localization because it does not contradict the better-characterized nuclear chromatin HAT activity. |
| GO:0005829 cytosol | HDA PMID:16823372 ORFeome cloning and global analysis of protein localization ... | KEEP AS NON CORE | Summary: The PomBase high-throughput cytosol row is retained as non-core. Reason: The cached ORFeome paper is abstract-only and does not show the per-protein image used by PomBase, but there is no basis to overrule the curator. Treat cytosol as a secondary localization relative to Mst2's nuclear chromatin activity. |
| GO:0006355 regulation of DNA-templated transcription | IEA GO_REF:0000002 | ACCEPT | Summary: This InterPro MYST-domain IEA is broad but consistent with Mst2-mediated chromatin acetylation. Reason: Mst2 is a MYST-family histone acetyltransferase, and H3K14 acetylation by Mst2 and Gcn5 modulates chromatin accessibility. The IEA is generic, but it is concordant with the PAINT-supported RNA polymerase II transcription row and does not overstate a paralog-specific function. Supporting Evidence: PMID:16199868 Mst2p is a negative regulator of silencing at the telomere but does not affect silencing in the centromere or mating type region. |
| GO:0006357 regulation of transcription by RNA polymerase II | IBA GO_REF:0000033 | ACCEPT | Summary: The broad MYST-family Pol II transcription term is appropriate for a chromatin histone acetyltransferase. Reason: PTN004172926 transfers a generic regulatory process that fits Mst2's role as a MYST-family chromatin acetyltransferase. The row is intentionally less specific than the H3K14 HAT and Mst2-complex annotations. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN004172926 · PTN004172926 SUPPORTS TRANSFER This root MYST-family process term is generic and compatible with Mst2's chromatin acetylation; narrower NuA4/SAS-I terms are on sibling nodes and are not propagated here. Supporting Evidence: PMID:39096900 targeting of chromodomain-fused Mst2 HAT to H3K9me-coated domains increases H3K14ac and SWI/SNF-dependent destabilization of heterochromatin. |
| GO:0031507 heterochromatin formation | IEA GO_REF:0000117 | MODIFY | Summary: Mst2 acts on the heterochromatin axis, but as an antagonist of H3K9 heterochromatin expansion rather than a factor that forms heterochromatin. Reason: Later direct evidence resolves the sign of this ARBA prediction. Mst2-mediated H3K14 acetylation counteracts the H3K14ub-H3K9me3 feedback loop and restrains heterochromatin spreading, so the replacement should name negative regulation of heterochromatin organization. Proposed replacements: negative regulation of heterochromatin organization Supporting Evidence: PMID:41786738 Mst2-mediated H3K14ac counteracts Clr3-mediated H3K14 deacetylation, therefore inhibiting H3K14ub, while Epe1 directly erases H3K9me3 |
| GO:0031507 heterochromatin formation | IGI PMID:21289066 Elimination of a specific histone H3K14 acetyltransferase co... | MODIFY | Summary: The 2011 RNAi-bypass phenotype supports an anti-silencing role for Mst2, not direct promotion of heterochromatin formation. Reason: The PomBase IGI row rests on the same heterochromatin biology captured by GO:0120262. Eliminating Mst2 H3K14 acetyltransferase activity bypasses the RNAi requirement for pericentric heterochromatin functions; this means wild-type Mst2 antagonizes, rather than builds, H3K9me-dependent heterochromatin. Proposed replacements: negative regulation of heterochromatin organization Supporting Evidence: PMID:21289066 when the activity of the histone H3 Lys 14 (H3K14) acetyltransferase Mst2 is eliminated, the RNAi machinery is no longer required for pericentric heterochromatin functions PMID:41786738 Together, these findings demonstrate that Mst2 and Epe1 function as independent brakes that restrain the H3K14ub-H3K9me3 feedback loop and prevent uncontrolled heterochromatin expansion. |
| GO:0033696 heterochromatin boundary formation | IGI PMID:25774602 Rapid epigenetic adaptation to uncontrolled heterochromatin ... | ACCEPT | Summary: Mst2 and Epe1 act redundantly to restrain heterochromatin spreading and ectopic heterochromatin assembly. Reason: Although Mst2 is not required for the IRC1R DNA boundary, it limits spreading at heterochromatin regions whose borders are set by chromatin-state balance rather than sequence-defined boundary elements. This is exactly the Mst2/Epe1 anti-spreading role that PomBase curates with GO:0033696. Supporting Evidence: PMID:25774602 In this study, we show that Mst2 regulates histone turnover at heterochromatin regions and that loss of Mst2 results in heterochromatin spreading at telomeres and heterochromatin islands where boundaries are absent. |
| GO:0033696 heterochromatin boundary formation | IGI PMID:39094565 Mapping the dynamics of epigenetic adaptation in S. pombe du... | ACCEPT | Summary: Mst2 is paired with Epe1 as an H3K9me antagonist in the induced heterochromatin-misregulation system. Reason: The 2024 adaptation study uses acute Epe1 and Mst2 depletion to trigger uncontrolled H3K9me redistribution, reinforcing that Mst2 contributes to the anti-spreading machinery that limits heterochromatin domains. Supporting Evidence: PMID:39094565 Deleting two major H3K9me antagonists – the H3K14 histone acetyltransferase Mst2 and the putative H3K9 demethylase Epe1 – leads to the adaptive silencing of the sole H3K9 methyltransferase, Clr4 |
| GO:0036408 histone H3K14 acetyltransferase activity | TAS PMID:21289066 Elimination of a specific histone H3K14 acetyltransferase co... | ACCEPT | Summary: Mst2 catalyzes nucleosomal histone H3K14 acetylation. Reason: The cached 2011 paper is abstract-only, but PomBase's TAS row is concordant with full-text 2012 Mst2-complex biochemistry demonstrating that Mst2 is the catalytic subunit and that H3K14 is the major substrate. Supporting Evidence: PMID:22184112 These results demonstrate that the Mst2 complex is a highly specific nucleosomal histone H3K14 acetyltransferase. |
| GO:0036410 Mst2 histone acetyltransferase complex | TAS PMID:21289066 Elimination of a specific histone H3K14 acetyltransferase co... | ACCEPT | Summary: Mst2 is the catalytic subunit of the fission-yeast Mst2 histone acetyltransferase complex. Reason: The exact fission-yeast complex term should be retained. Full-text Mst2-FLAG and Pdp3-FLAG purifications identified a stable Mst2 complex whose integrity is required for H3K14 acetyltransferase activity. Supporting Evidence: PMID:22184112 Purification of Mst2-FLAG and mass spectrometry analysis identified identical components |
| GO:0061733 protein-lysine-acetyltransferase activity | IEA GO_REF:0000120 | ACCEPT | Summary: The EC/Rhea lysine-acetyltransferase parent captures the chemistry of Mst2-dependent histone acetylation. Reason: Mst2 transfers an acetyl group to the epsilon amino group of a lysine in histone H3K14, so the generic protein-lysine-acetyltransferase activity inferred by EC/Rhea is correct. Supporting Evidence: PMID:22184112 These results demonstrate that the Mst2 complex is a highly specific nucleosomal histone H3K14 acetyltransferase. |
| GO:0061733 protein-lysine-acetyltransferase activity | ISS GO_REF:0000024 | ACCEPT | Summary: The human-KAT8 ISS row transfers only generic lysine acetyltransferase chemistry, which Mst2 has. Reason: The donor is a MYST-family paralog, but the term is not KAT8-specific. It asserts only protein-lysine-acetyltransferase activity, and Mst2 directly catalyzes that chemistry on histone H3K14. Supporting Evidence: PMID:22184112 These results demonstrate that the Mst2 complex is a highly specific nucleosomal histone H3K14 acetyltransferase. |
| GO:0070775 H3 histone acetyltransferase complex | IEA GO_REF:0000117 | MODIFY | Summary: Mst2 is part of an H3 HAT complex, but the exact fission-yeast term is available. Reason: The ARBA prediction is directionally correct but too general. Mst2 is the catalytic subunit of the named Mst2 histone acetyltransferase complex that is already present in PomBase. Proposed replacements: Mst2 histone acetyltransferase complex Supporting Evidence: PMID:22184112 Purification of Mst2-FLAG and mass spectrometry analysis identified identical components |
| GO:0120261 regulation of heterochromatin organization | IEA GO_REF:0000117 | ACCEPT | Summary: This broad ARBA term correctly covers Mst2's antagonism of heterochromatin expansion. Reason: The IDA row to the child GO:0120262 captures the direction more precisely, but the parent regulation term is entailed and should be retained. Supporting Evidence: PMID:41786738 Together, these findings demonstrate that Mst2 and Epe1 function as independent brakes that restrain the H3K14ub-H3K9me3 feedback loop and prevent uncontrolled heterochromatin expansion. |
| GO:0120262 negative regulation of heterochromatin organization | IDA PMID:39096900 Nucleosome remodeler exclusion by histone deacetylation enfo... | ACCEPT | Summary: Mst2-dependent H3K14 acetylation destabilizes heterochromatin by favoring SWI/SNF-family remodeler access and histone turnover. Reason: The 2024 Mol Cell paper directly tested targeted Mst2 recruitment to H3K9me-coated domains and found higher H3K14ac, SWI/SNF recruitment, defective heterochromatin propagation, and subtelomeric loss of H3K9me3. This agrees with the older Mst2/Epe1 genetics and the 2026 H3K14ub-H3K9me3 feedback model. Supporting Evidence: PMID:39096900 targeting of chromodomain-fused Mst2 HAT to H3K9me-coated domains increases H3K14ac and SWI/SNF-dependent destabilization of heterochromatin. |
| GO:1990467 NuA3a histone acetyltransferase complex | IBA GO_REF:0000033 | MODIFY | Summary: The fungal PAINT node is sound for budding-yeast SAS3/NuA3a, but fission yeast has the related, distinct Mst2 complex. Reason: PTN008308138 carries a GO:1990467 NuA3a assertion seeded by S. cerevisiae SAS3. Fission-yeast Mst2 sits in the same PTHR10615:SF161 subfamily and has NuA3-like activity, but Wang et al. showed that its complex differs from budding yeast NuA3, lacks the Yng1 subunit, and contains the fission-specific Ptf1 and Ptf2 subunits. The exact replacement is the PomBase term for the Mst2 histone acetyltransferase complex. Propagation Review Root cause: PROPAGATION BAD Failure modes: COMPARTMENT OR COMPLEX MISMATCH GRANULARITY MISMATCH Sources checked: PANTHER:PTN008308138 · PTN008308138 SUPPORTS SOURCE BUT NOT TARGET The fungal node is correctly seeded by budding-yeast SAS3/NuA3a, but fission yeast has a related Mst2 complex with different subunit composition; the exact term for mst2 is GO:0036410. Proposed replacements: Mst2 histone acetyltransferase complex Supporting Evidence: PMID:22184112 The subunit composition of fission yeast Mst2 complex is slightly different from that of NuA3 file:interpro/panther/PTHR10615/PTHR10615-paint.tsv PTHR10615 PTN008308138 GO:1990467 C IBD false SGD:S000000148 taxon:4751 20230926 |
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